Evidence map›Paper›PMID 21397190›Full record

ArticleStructure (London, England : 1993)2011

X-ray crystal structure of the UCS domain-containing UNC-45 myosin chaperone from Drosophila melanogaster.

Chi F Lee, Arthur V Hauenstein, Jonathan K Fleming, William C Gasper, Valerie Engelke, Banumathi Sankaran, Sanford I Bernstein, Tom Huxford

Open access · bronzeAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
2.3field-weighted citation impact, top 12% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

25 citing papers in PubMed, 38 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Unconventional Myosins fromBiomolecules · 2022
    Review
  5. Putting AlphaFold models to work with phenix.process_predicted_model and ISOLDE.Acta crystallographica. Section D, Structural biology · 2022
    Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Metazoan evolution of the armadillo repeat superfamily.Cellular and molecular life sciences : CMLS · 2017
    Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Myosin chaperones.Current opinion in structural biology · 2014
    Review
  20. The UNC-45 myosin chaperone: from worms to flies to vertebrates.International review of cell and molecular biology · 2014
    Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors at 2 institutions in 1 country.

Chi F LeeDepartment of Biology, San Diego State University, 5500 Campanile Drive, San Diego, CA 92182-1030, USA.
Arthur V Hauenstein
Jonathan K Fleming
William C Gasper
Valerie Engelke
Banumathi Sankaran
Sanford I Bernstein
Tom Huxford
San Diego State University · USLawrence Berkeley National Laboratory · US

Funding

THE INTERSECTION OF LANGUAGE AND AFFECTR25GM058906 · NIGMS · SAN DIEGO STATE UNIVERSITY · PI TONG, WILLIAM G. · 1999 to 2021
$10.7M
Strucutre of the UNC-45 Chaperone and its Interaction with Skeletal Muscle MyosinR01AR055958 · NIAMS · SAN DIEGO STATE UNIVERSITY · PI BERNSTEIN, SANFORD I · 2008 to 2017
$2.5M
NIAMS NIH HHS R01 AR055958NIAMS NIH HHS R01-AR055958NIGMS NIH HHS R25 GM058906
6 · The paper itself

Abstract

UCS proteins, such as UNC-45, influence muscle contraction and other myosin-dependent motile processes. We report the first X-ray crystal structure of a UCS domain-containing protein, the UNC-45 myosin chaperone from Drosophila melanogaster (DmUNC-45). The structure reveals that the central and UCS domains form a contiguous arrangement of 17 consecutive helical layers that arrange themselves into five discrete armadillo repeat subdomains. Small-angle X-ray scattering data suggest that free DmUNC-45 adopts an elongated conformation and exhibits flexibility in solution. Protease sensitivity maps to a conserved loop that contacts the most carboxy-terminal UNC-45 armadillo repeat subdomain. Amino acid conservation across diverse UCS proteins maps to one face of this carboxy-terminal subdomain, and the majority of mutations that affect myosin-dependent cellular activities lie within or around this region. Our crystallographic, biophysical, and biochemical analyses suggest that DmUNC-45 function is afforded by its flexibility and by structural integrity of its UCS domain.

Indexed as

Amino Acid SequenceAnimalsArmadillo Domain ProteinsCaenorhabditis elegansCrystallography, X-RayDrosophila melanogasterDrosophila ProteinsEscherichia coliModels, MolecularMolecular ChaperonesMolecular Sequence DataMutationMyosinsPliabilityProtein Structure, SecondaryProtein Structure, TertiaryArmadillo Domain ProteinsDrosophila ProteinsMolecular ChaperonesMyosinsRecombinant ProteinsUNC-45 protein, Drosophila

Identifiers

PMID21397190
PMCPMC3060410
OpenAlexW1988139565

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.